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Database: UniProt
Entry: A0A091P5R1_LEPDC
LinkDB: A0A091P5R1_LEPDC
Original site: A0A091P5R1_LEPDC 
ID   A0A091P5R1_LEPDC        Unreviewed;       344 AA.
AC   A0A091P5R1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Protein RMD5 A {ECO:0000313|EMBL:KFQ02498.1};
DE   Flags: Fragment;
GN   ORFNames=N330_02709 {ECO:0000313|EMBL:KFQ02498.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ02498.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ02498.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ02498.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR   EMBL; KK667903; KFQ02498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091P5R1; -.
DR   PhylomeDB; A0A091P5R1; -.
DR   Proteomes; UP000053001; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd16794; dRING_RMD5A; 1.
DR   InterPro; IPR013144; CRA_dom.
DR   InterPro; IPR024964; CTLH/CRA.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR045098; Fyv10_fam.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR037680; RMD5A_dRING.
DR   InterPro; IPR044063; ZF_RING_GID.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   PANTHER; PTHR12170:SF5; E3 UBIQUITIN-PROTEIN TRANSFERASE RMND5A; 1.
DR   PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR   Pfam; PF10607; CTLH; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS51867; ZF_RING_GID; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01215}.
FT   DOMAIN          106..163
FT                   /note="CTLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50897"
FT   DOMAIN          289..330
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51867"
FT   ZN_FING         289..330
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ02498.1"
FT   NON_TER         344
FT                   /evidence="ECO:0000313|EMBL:KFQ02498.1"
SQ   SEQUENCE   344 AA;  38658 MW;  B7266589F17EAD4E CRC64;
     DQDGDLSGTI SLVMTQCCKR IKDTVQKLAS DHKDIHSSVS RVGKAIDKNF DSDISSVGID
     GCWQADSQRI LNEVMVEHFF RQGMLDVAEE LCQESGLSID QSQKEPFVEL NRILEALKVR
     VLRPALEWAV SNREMLMAQN SSLEFKLHRL YFISLLMGGT ANQREALQYA KNFQPFALNH
     QKDIQVLMGS LVYLRQGIEN SPYVHLLDAN QWADICDIFT RDACALLGLS VESPLSVSFS
     AGCVALPALI NIKAVIEQRQ CTGVWNQKDE LPIEVDLGKK CWYHSIFACP ILRQQTTDNN
     PPMKLVCGHI ISRDALNKMF NGSKLKCPYC PMEQSPGDAK QIFF
//
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